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1j30

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(New page: 200px<br /><applet load="1j30" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j30, resolution 1.70&Aring;" /> '''The crystal structur...)
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[[Image:1j30.gif|left|200px]]<br /><applet load="1j30" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1j30, resolution 1.70&Aring;" />
caption="1j30, resolution 1.70&Aring;" />
'''The crystal structure of sulerythrin, a rubrerythrin-like protein from a strictly aerobic and thermoacidiphilic archaeon'''<br />
'''The crystal structure of sulerythrin, a rubrerythrin-like protein from a strictly aerobic and thermoacidiphilic archaeon'''<br />
==Overview==
==Overview==
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Sulerythrin is the first rubrerythrin-like protein to be isolated from an, aerobic organism, Sulfolobus tokodaii strain 7, and it lacks a C-terminal, rubredoxin-like FeS(4) domain. The protein purified from Sulfolobus cells, was crystallized, and the crystal structure was determined at 1.7 A, resolution. The dimer of sulerythrin exhibited "domain-swapping" at the, loop connecting alphaB and alphaC, hybrid four-helix bundles consisting of, alphaA/B and alphaC/D being formed. The structure and atomic identity of, the binuclear metal center were determined by means of anomalous, scattering analysis. The site contained 1.0 mol of hexacoordinate Fe, 0.80-0.87 mol of tetracoordinate Zn, and 0.73-0.88 mol of putative O(2), per monomer. The metal ions were found at exchanged positions compared to, those in the Fe/Zn-containing rubrerythrin from Desulfovibrio vulgaris., The results demonstrate that the binuclear metal center of, rubrerythrin-like proteins is plastic in its ability to bind metal ions.
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Sulerythrin is the first rubrerythrin-like protein to be isolated from an aerobic organism, Sulfolobus tokodaii strain 7, and it lacks a C-terminal rubredoxin-like FeS(4) domain. The protein purified from Sulfolobus cells was crystallized, and the crystal structure was determined at 1.7 A resolution. The dimer of sulerythrin exhibited "domain-swapping" at the loop connecting alphaB and alphaC, hybrid four-helix bundles consisting of alphaA/B and alphaC/D being formed. The structure and atomic identity of the binuclear metal center were determined by means of anomalous scattering analysis. The site contained 1.0 mol of hexacoordinate Fe, 0.80-0.87 mol of tetracoordinate Zn, and 0.73-0.88 mol of putative O(2) per monomer. The metal ions were found at exchanged positions compared to those in the Fe/Zn-containing rubrerythrin from Desulfovibrio vulgaris. The results demonstrate that the binuclear metal center of rubrerythrin-like proteins is plastic in its ability to bind metal ions.
==About this Structure==
==About this Structure==
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1J30 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_tokodaii Sulfolobus tokodaii] with FE, ZN and OXY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1J30 OCA].
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1J30 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_tokodaii Sulfolobus tokodaii] with <scene name='pdbligand=FE:'>FE</scene>, <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=OXY:'>OXY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J30 OCA].
==Reference==
==Reference==
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[[Category: sulfolobus tokodaii strain 7]]
[[Category: sulfolobus tokodaii strain 7]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:00:34 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:18:21 2008''

Revision as of 11:18, 21 February 2008


1j30, resolution 1.70Å

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The crystal structure of sulerythrin, a rubrerythrin-like protein from a strictly aerobic and thermoacidiphilic archaeon

Overview

Sulerythrin is the first rubrerythrin-like protein to be isolated from an aerobic organism, Sulfolobus tokodaii strain 7, and it lacks a C-terminal rubredoxin-like FeS(4) domain. The protein purified from Sulfolobus cells was crystallized, and the crystal structure was determined at 1.7 A resolution. The dimer of sulerythrin exhibited "domain-swapping" at the loop connecting alphaB and alphaC, hybrid four-helix bundles consisting of alphaA/B and alphaC/D being formed. The structure and atomic identity of the binuclear metal center were determined by means of anomalous scattering analysis. The site contained 1.0 mol of hexacoordinate Fe, 0.80-0.87 mol of tetracoordinate Zn, and 0.73-0.88 mol of putative O(2) per monomer. The metal ions were found at exchanged positions compared to those in the Fe/Zn-containing rubrerythrin from Desulfovibrio vulgaris. The results demonstrate that the binuclear metal center of rubrerythrin-like proteins is plastic in its ability to bind metal ions.

About this Structure

1J30 is a Single protein structure of sequence from Sulfolobus tokodaii with , and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of sulerythrin, a rubrerythrin-like protein from a strictly aerobic archaeon, Sulfolobus tokodaii strain 7, shows unexpected domain swapping., Fushinobu S, Shoun H, Wakagi T, Biochemistry. 2003 Oct 14;42(40):11707-15. PMID:14529281

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